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3D Reconstruction of Smooth Muscle A-Actinin by Cryo Electron Microscopy

Published online by Cambridge University Press:  02 July 2020

Jun Liu ,
Dianne Taylor  and
Kenneth A. Taylor
Jun Liu
Affiliation:
Institute of Molecular Biophysics, Florida State University, Tallahassee, FL32306
Dianne Taylor
Affiliation:
Institute of Molecular Biophysics, Florida State University, Tallahassee, FL32306
Kenneth A. Taylor
Affiliation:
Institute of Molecular Biophysics, Florida State University, Tallahassee, FL32306
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Extract

α-Actinin is an actin crosslinking protein identified in a wide variety of cells. Both muscle and nonmuscle isoforms of α-actinin have been characterized [1]. The molecule consists of two polypeptide chains that form a rod-shaped antiparallel dimer. Each polypeptide is composed of three distinct structural regions: actin-binding domain, four triple helical repeats that form a central rod, and a carboxyl terminal domain that contains two EF hand calcium-binding sites. Here we present the 3D structure of the smooth muscle α-actinin, as determined by cryo electron microscopy at 2.0 nm resolution.

Two dimensional crystals of chicken gizzard α-actinin were formed on positively charged lipid monolayer [2] and preserved frozen hydrated for TEM. The crystal has a unit cell dimension of a = 26.31 nm, b = 20.37 nm, γ= 107.10°, based on internal calibration against TMV.

Type
Electron Cryomicroscopy of Macromolecules
Information
Microscopy and Microanalysis , Volume 6 , Issue S2: Proceedings: Microscopy & Microanalysis 2000, Microscopy Society of America 58th Annual Meeting, Microbeam Analysis Society 34th Annual Meeting, Microscopical Society of Canada/Societe de Microscopie de Canada 27th Annual Meeting, Philadelphia, Pennsylvania August 13-17, 2000 , August 2000 , pp. 244 - 245
Copyright
Copyright © Microscopy Society of America

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References

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